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Peroxiredoxin-5, mitochondrial (EC 1.11.1.15) (Antioxidant enzyme B166) (AOEB166) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (Thioredoxin peroxidase PMP20)

 PRDX5_RAT               Reviewed;         213 AA.
Q9R063; Q68G22;
21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 125.
RecName: Full=Peroxiredoxin-5, mitochondrial;
EC=1.11.1.15;
AltName: Full=Antioxidant enzyme B166;
Short=AOEB166;
AltName: Full=PLP;
AltName: Full=Peroxiredoxin V;
Short=Prx-V;
AltName: Full=Peroxisomal antioxidant enzyme;
AltName: Full=Thioredoxin peroxidase PMP20;
Flags: Precursor;
Name=Prdx5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
Duconseille E., Falmagne P., Bernard A.;
"Cloning and characterization of AOEB166, a novel mammalian
antioxidant enzyme of the peroxiredoxin family.";
J. Biol. Chem. 274:30451-30458(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-130.
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 75-82; 86-115 AND 159-176, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events.
{ECO:0000269|PubMed:10521424}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:P30044}.
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30044}.
-!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion
{ECO:0000250|UniProtKB:P30044}.
-!- SUBCELLULAR LOCATION: Isoform Cytoplasmic+peroxisomal: Cytoplasm
{ECO:0000250|UniProtKB:P30044}. Peroxisome matrix
{ECO:0000250|UniProtKB:P30044}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Mitochondrial;
IsoId=Q9R063-1; Sequence=Displayed;
Name=Cytoplasmic+peroxisomal;
IsoId=Q9R063-2; Sequence=VSP_018832;
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this atypical 2-Cys Prx, C(R) is present in the same
subunit to form an intramolecular disulfide. The disulfide is
subsequently reduced by thioredoxin.
{ECO:0000250|UniProtKB:P30044}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF110732; AAF03751.1; -; mRNA.
EMBL; BC078771; AAH78771.1; -; mRNA.
RefSeq; NP_446062.1; NM_053610.1. [Q9R063-1]
UniGene; Rn.2944; -.
ProteinModelPortal; Q9R063; -.
BioGrid; 250207; 1.
IntAct; Q9R063; 1.
STRING; 10116.ENSRNOP00000028687; -.
PeroxiBase; 4452; RnoPrxV.
iPTMnet; Q9R063; -.
PhosphoSitePlus; Q9R063; -.
SwissPalm; Q9R063; -.
PaxDb; Q9R063; -.
PRIDE; Q9R063; -.
GeneID; 113898; -.
KEGG; rno:113898; -.
UCSC; RGD:71007; rat. [Q9R063-1]
CTD; 25824; -.
RGD; 71007; Prdx5.
eggNOG; KOG0541; Eukaryota.
eggNOG; COG0678; LUCA.
HOGENOM; HOG000255884; -.
HOVERGEN; HBG053675; -.
InParanoid; Q9R063; -.
KO; K11187; -.
PhylomeDB; Q9R063; -.
TreeFam; TF105182; -.
BRENDA; 1.11.1.15; 5301.
PRO; PR:Q9R063; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
GO; GO:0005739; C:mitochondrion; IDA:HGNC.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0005782; C:peroxisomal matrix; ISO:RGD.
GO; GO:0005777; C:peroxisome; IDA:HGNC.
GO; GO:0016209; F:antioxidant activity; ISO:RGD.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:RGD.
GO; GO:0004601; F:peroxidase activity; ISO:RGD.
GO; GO:0051920; F:peroxiredoxin activity; ISO:RGD.
GO; GO:0072541; F:peroxynitrite reductase activity; ISO:RGD.
GO; GO:0046983; F:protein dimerization activity; ISO:RGD.
GO; GO:0005102; F:receptor binding; ISO:RGD.
GO; GO:0001016; F:RNA polymerase III regulatory region DNA binding; ISO:RGD.
GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:RGD.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
GO; GO:0070995; P:NADPH oxidation; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0051354; P:negative regulation of oxidoreductase activity; ISO:RGD.
GO; GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; ISO:RGD.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:RGD.
GO; GO:2001057; P:reactive nitrogen species metabolic process; ISO:RGD.
GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; ISO:RGD.
GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Acetylation; Alternative initiation; Antioxidant; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion;
Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein; Polymorphism;
Redox-active center; Reference proteome; Transit peptide.
TRANSIT 1 51 Mitochondrion. {ECO:0000255}.
CHAIN 52 213 Peroxiredoxin-5, mitochondrial.
/FTId=PRO_0000023799.
DOMAIN 55 213 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 211 213 Microbody targeting signal.
{ECO:0000250|UniProtKB:P30044}.
ACT_SITE 99 99 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P30044}.
MOD_RES 74 74 N6-acetyllysine.
{ECO:0000250|UniProtKB:P99029}.
MOD_RES 82 82 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P30044}.
MOD_RES 82 82 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P99029}.
MOD_RES 115 115 N6-succinyllysine.
{ECO:0000250|UniProtKB:P99029}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000250|UniProtKB:P99029}.
DISULFID 99 203 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 1 51 Missing (in isoform
Cytoplasmic+peroxisomal). {ECO:0000305}.
/FTId=VSP_018832.
VARIANT 68 68 E -> G.
VARIANT 114 114 L -> P.
VARIANT 130 130 A -> V. {ECO:0000269|PubMed:15489334}.
SEQUENCE 213 AA; 22179 MW; 9F0D03A4CC87708A CRC64;
MVQLRFCVLG SIAGSVLRAS ATWTCVAGRA GRKGAGWECG GARSFSSAAV TMAPIKVGDT
IPSVEVFEGE PGKKVNLAEL FKDKKGVLFG VPGAFTPGCS KTHLPGFVEQ AGALKAKGAQ
VVACLSVNDA FVTAEWGRAH QAEGKVQLLA DPTGAFGKET DLLLDDSLVS LFGNRRLKRF
SMVIDKGVVK ALNVEPDGTG LTCSLAPNIL SQL


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